Research workbench
Murine inducible nitric oxide synthase oxygenase domain (delta 114) 4-(imidazol-1-YL)PHENOL and piperonylamine complex
Analyse Murine inducible nitric oxide synthase oxygenase domain (delta 114)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ORQ
- Type
- protein
- Length
- 300 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitric oxide synthase, inducible
- EC
- 1.14.13.39
- UniProt
- P29477
- Ligands
- HEM, MSR, MR1
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitric oxide synthase, inducible (EC 1.14.13.39) | protein | 300 | 38% helix, 16% strand | P29477 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- MSR · 4-(1H-imidazol-1-yl)phenol · ligand · chains A
- MR1 · 1-(1,3-benzodioxol-5-yl)methanamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.68 | 0.81 | 34 | HEM, MSR |
| 2 | 90 | 0.46 | 0.80 | 19 | empty |
| 3 | 127 | 0.39 | 0.74 | 23 | empty |
| 4 | 71 | 0.38 | 0.78 | 22 | empty |
| 5 | 52 | 0.38 | 0.80 | 19 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2ORQ · Murine Inducible Nitric Oxide Synthase Oxygenase Domain (DELTA 114)… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P29477
- Elsewhere: RCSB PDB 2ORQ · PDBe 2ORQ · UniProt P29477
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